A Bruker Fourier transform NMR has been augmented with data handling equipment to increase its power sensitivity four times, allow protein proton NMR in H2O solvent, and control automated double resonance. It is likely that we will study transaminases by substrate T2 and measure O2 binding kinetics in hemoglobin by transient NMR. Exchange rates of amino and amide protons in enzymes, nucleic acids, and model systems thereof, are also under study, as well as electron transfer kinetics and electronic structure of cytochrome-c from various sources.